Disease relevance of cg0250

• Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum [1].
• Amiclenomycin (AM) was found to be a strong inhibitor of KAPA-DAPA aminotransferase of Brevibacterium divaricatum [2].
• The predicted DapC protein of C. glutamicum shared 29% identical amino acids with DapC from Bordetella pertussis, the only enzymatically characterized N-succinyl-aminoketopimelate aminotransferase [3].

High impact information on cg0250

• Twenty putative aminotransferase (AT) proteins of Corynebacterium glutamicum, or rather pyridoxal-5'-phosphate (PLP)-dependent enzymes, were isolated and assayed among others with L-glutamate, L-aspartate, and L-alanine as amino donors and a number of 2-oxo-acids as amino acceptors [1].
• At 0.1 mM concentrations of phenylhydrazine, 90% inhibitions of aminotransferase activities were achieved in partially purified preparations of B. flavum and C. glutamicum [4].
• Pretyrosine is formed from prephenate via the activity of at least one species of aromatic aminotransferase which is significantly greater with prephenate as substrate than with either phenylpyruvate or 4-hydroxyphenylpyruvate [5].
• Overexpression of the dapC gene in C. glutamicum resulted in a 9-fold increase of the specific aminotransferase activity [3].
• The novel protein with aminotransferase activity in valine biosynthesis belongs to the very recently described MocR subfamily of GntR-type helix-turn-helix transcriptional regulators, is located upstream of a potential operon of a newly described pyridoxine biosynthetic pathway and when disrupted, gives rise to a pyridoxine auxotrophy [6].

Biological context of cg0250

• These facts indicate that AM exerts its inhibitory action against KAPA-DAPA aminotransferase by binding to the enzyme, probably to the KAPA-DAPA binding site [2].

References